Molecular Playground/Saposin C

One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground

Saposin C domain of prosaposin
Prosaposin is a precursor of four cofactors, saposins A, B,C and D, which are required for hydrolysis of sphingolipids by lysosomal enzymes (1). Prosaposin contains multiple glycans and was found to be an obligate substrate for the UDP-glucose:glycoprotein glucosyl transferase 1 (UGT1), a folding sensor that resides in the ER and supports folding of secretory proteins(1). Deficiency of UGT1 causes defects in prosaposin maturation(1). Prosaposin is cleaved in the lysosome into the four saposins. The four saposins are members of the larger family of saposin –like proteins(2). The saposin motif is characterized by six cysteines  that form three intramolecular disulfide bonds(2). In this representation is shown the saposin C domain of prosaposin. Saposin C adopts a monomeric saposin fold with four amphipathic  α-helices,  where the third helix shows a highly  localized kink (2).